菊苣根提取物的抑菌活性研究

采用离体的试验方法测定了菊苣根的石油醚、乙酸乙酯和乙醇提取物对7种植物病原真菌和3种细菌的抑制活性。采用盆栽试验方法测定了菊苣根提取物对小麦白粉病的防治效果。结果表明,乙醇和乙酸乙酯提取物均有一定的抑制植物病原真菌和细菌活性。且乙酸乙酯提取物效果更佳。在10 g.L-1浓度下,乙酸乙酯提取物能显著抑制小麦赤霉病菌、玉米大斑病菌和烟草赤星病菌3种病原真菌菌丝的生长,抑制率均在85%以上;对小麦根腐病菌、玉米大斑病菌和烟草赤星病菌的孢子萌发抑制率也均在80%以上;对枯草芽孢杆菌和金黄色葡萄球菌的抑菌圈直径达21.01 mm和17.23 mm;对盆栽小麦白粉病的预防和治疗作用分别为50.93%和65.82%。     

菊苣提取物和菊粉降脂活性研究

以300日龄商品代尼克T粉壳蛋鸡为试验动物,研究了菊苣提取物和菊粉对血清脂质、蛋黄总脂和胆固醇的影响.结果显示,0.1%菊苣提取物组、2.0%菊苣提取物组和0.1%菊粉组血清胆固醇(TC)、甘油三脂(TG)、低密度脂蛋白(LDL-C)均显著低于对照组(P<0.05),其中0.1%菊苣提取物组TC降低36.47%,TG降低40.71%,LDL-C降低36.09%,0.1%菊粉组LDL-C降低16.23%,差异极显著(P<0.01);2.0%菊苣提取物组高密度脂蛋白(HDL-C)比对照组高23.19%,差异极显著(P<0.01);2.0%菊苣提取物组蛋黄总脂和蛋黄胆固醇显著降低(P<0.05).表明菊苣提取物和菊粉均具有降血脂活性,但菊苣提取物比菊粉活性更强;菊苣提取物还具有降低蛋黄总脂和胆固醇的作用.     

华泽兰根化学成分及其抑制α-葡萄糖苷酶和蛋白酪氨酸磷酸酶1B的活性研究

为研究华泽兰Eupatorium chinense根部的化学成分及其抗糖尿病活性,采用正相硅胶柱色谱、薄层色谱、凝胶柱色谱及半制备高效液相色谱等色谱方法,从华泽兰根部分离得到15个单体化合物,并通过现代波谱技术鉴定其结构分别为：8S-9-hydroxythymol（1）、8,10-dehydro-9-hydroxythymol（2）、1-[4-hydroxy-3-methoxy-5-（3-methylbut-3-en-1-ynyl）phenyl]wethanone（3）、speciosin L（4）、（R）-8-hydroxy-9-isobutyryloxythymol（5）、1,4-[13C]-1,2,3,4-tetrahydro-5-naphthyl-amin（6）、eupatriol（7）、3β,6-hydroxytremetone（8）、泽兰酮（9）、（2R,3S）-5-acetyl-6-hydroxyl-2-isopropenyl-3-ethoxy-dihydrofuran（10）、（2R,3S）-5-乙酰基-6-羟基-2-异丙烯基-3-乙氧基-苯并二氢呋喃（11）、6-羟基-2H-苯并呋喃-3-酮（12）、3,5-dimethyl-2,3-dihydrobenzofuran（13）、2,4-bis-（5-acetyl-6-hydroxy-benzofuran-2-yl）-4-methyl-pent-1-ene（14）、1,1′-[[（2E）-4-methylpent-2-ene-2,4-diyl]bis（6-hydroxy-1-benzofuran-2,5-diyl）]diethanone（15）。其中化合物3为首次从泽兰属植物中分离获得,化合物14为首次从华泽兰中分离获得。采用对硝基苯基-β-吡喃半乳糖苷法与对硝基苯磷酸盐法分别测定所有化合物对诱导糖尿病发生的α-葡萄糖苷酶和蛋白酪氨酸磷酸酶1B（PTP1B）的抑制活性进行评价,化合物3、4、5和12具有良好的α-葡萄糖苷酶抑制活性,其IC₅₀值分别为3.7、10.1、21.3、22.5μg/mL,其中化合物3的抑制活性优于良性药阿卡波糖（4.6μg/mL）;化合物1、3、4和12具有良好的PTP1B抑制活性,其IC₅₀值分别为15.2、8.6、2.2和21.2μg/mL,其中化合物3的抑制活性优于良性药齐墩果酸（12.5μg/mL）,化合物4的抑制活性优于阳性药正钒酸钠（7.5μg/mL）和齐墩果酸（12.5μg/mL）。研究表明,炔类化合物3和4均具有较明显的α-葡萄糖苷酶和PTP1B抑制活性。利用分子对接技术计算化合物3和4分别与α-葡萄糖苷酶和PTP1B的相互作用,结果表明化合物3和4与α-葡萄糖苷酶和PTP1B均具有较强的结合力。本论文首次采用双靶点对华泽兰根部的化学成分进行了抗糖尿病活性及构效研究,发现化合物3和4可作为抗糖尿病的先导化合物。     

球毛壳菌H6次级代谢产物及其α-葡萄糖苷酶抑制活性

采用体外α-葡萄糖苷酶抑制模型对一株球毛壳菌H6的发酵液和菌丝体两种乙酸乙酯提取物进行活性评价,结果表明,发酵液乙酸乙酯提取物对α-葡萄糖苷酶具有较强的抑制活性,其IC₅₀值为(510.76±23.46)μg/mL。采用硅胶、Sephadex LH-20、半制备高效液相等色谱技术从其发酵液乙酸乙酯提取物中分离得到12个化合物。通过各种光谱分析,依次鉴定为chaetoviridins A-B(1-2),chaetoglobosins A-D(3-6),chaetoglobosin J(7),chaetoglobosin Q(8),prochaetogobosinsⅠ-Ⅲ(9-11),vibratilicin(12),其中化合物12为首次从毛壳属中分离得到。对化合物进行α-葡萄糖苷酶抑制活性测定发现,化合物12显示弱的抑制活性,其IC₅₀为(1 182.75±19.14)μg/mL。     

黄连提取物对α-葡萄糖苷酶抑制作用研究

利用体外α-葡萄糖苷酶抑制模型对黄连不同部位提取物进行活性评价,并与阳性对照Acarbose比较,发现黄连不同部位均有一定的α-葡萄糖苷酶抑制活性.其中,黄连根茎乙酸乙酯提取物的抑制活性最高(IC_(50)=20.72 μg/mL),黄连种子石油醚部位(IC_(50)=40.86 μg/mL)和黄连叶石油醚部位(IC_(50)=62.85 μg/mL)的活性次之.3个部位的提取物活性均远大于阳性对照Acarbose(IC_(50)=1081,27 μg/mL).不同部位比较,根茎对α-葡萄糖苷酶抑制活性最好,这3种提取物抑制活性均比阳性对照高;同一部位不同提取物比较,石油醚和甲醇提取物α-葡萄糖苷酶抑制活性一般要高于乙酸乙酯提取物.     

基于靶向代谢组学技术研究毛菊苣对肥胖小鼠粪便胆汁酸谱的影响

目的 探究毛菊苣乙醇提取物对高脂饮食诱导的肥胖小鼠粪便胆汁酸谱的影响。方法 选取6周龄C57BL/6雄性小鼠24只随机分为正常组、模型组、给药组和二甲双胍组。正常组给予常规饮食,其余3组给予高脂饲料,同时给药组每日灌胃10 mL/kg毛菊苣乙醇提取物溶液,二甲双胍组每日灌胃10 mL/kg二甲双胍溶液。10周后收集小鼠肝检测肝甘油三酯（triglycerides, TG）、总胆固醇（total cholesterol, TC）、低密度脂蛋白胆固醇（low-density lipoprotein cholesterol, LDL-C）和高密度脂蛋白胆固醇（high-density lipoprotein cholesterol, HDL-C）;收集小鼠粪便通过超高效液相色谱-串联质谱法（ultra performance liquid chromatography-tandem mass spectrometry, UPLC-MS/MS）检测粪便胆汁酸含量。结果 与正常组相比,模型组小鼠体重（P<0.0001）、血清TG、TC、LDL-C水平（P<0.0001）和肝TG水平（P<0.05）显著升高,肝HDL-C水平显著降低（P<0.001）,表现出增重和脂质代谢异常。毛菊苣乙醇提取物能显著降低小鼠体重（P<0.0001）、血清TG（P<0.05）、TC（P<0.01）、LDL-C（P<0.01）水平及肝TG（P<0.0001）、LDL-C（P<0.05）水平。方法学验证结果表明本研究建立的方法能准确定量粪便中的52种胆汁酸。分析各类胆汁酸浓度发现,毛菊苣乙醇提取物能显著增大次级胆汁酸/初级胆汁酸比例（P<0.05）。多元统计分析结果显示,各组的胆汁酸代谢模式发生明显改变。以第一主成分的变量投影重要度（variable importance in the projection, VIP）>1,P<0.05为条件筛选出给药组相对模型组的8种差异胆汁酸。通过检索京都基因与基因组百科全书（Kyoto Encyclopedia of Genes and Genomes, KEGG）数据库,发现差异胆汁酸主要参与次级胆汁酸生物合成途径。相关分析表明,粪便中脱氧胆酸（r_s=0.6445,P<0.001）、异石胆酸（r_s=0.5879,P<0.01）、3β-脱氧胆酸（r_s=0.6649,P<0.001）和ω-鼠胆酸（r_s=0.5387,P<0.01）4种差异胆汁酸与体重具有较强的正相关。结论 毛菊苣乙醇提取物可能通过调控次级胆汁酸生物合成,改变粪便胆汁酸代谢轮廓从而发挥减重和改善脂质异常的作用。     

人面果叶子、根部、果实提取物体外抗糖尿病活性研究(英文)

为了评价人面果叶子、根部、果实提取物体外抗糖尿病活性,相应测定了其石油醚提取物(PFr.)、乙酸乙酯提取物(EFr.)、正丁醇提取物(BFr.)、水提取物(WFr.)的α-葡萄糖苷酶与α-淀粉酶抑制活性,以及HepG2细胞的促葡萄糖消耗能力。果实乙酸乙酯提取物(IC50=17.81±1.09μg/mL)、叶子乙酸乙酯提取物(IC50=18.60±1.56μg/mL)、根部乙酸乙酯提取物(IC50=14.05±0.24μg/mL)、根部正丁醇提取物(IC50=13.01±0.38μg/mL)显示了较好的α-葡萄糖苷酶抑制活性(acarbose IC50200μg/mL)。而根部乙酸乙酯与正丁醇提取物在600μg/mL的浓度下就显示了90%的α-葡萄糖苷酶抑制率,在1.5 mg/mL的浓度下显示了90%的α-淀粉酶抑制率。在促葡萄糖消耗试验中,果实乙酸乙酯提取物在浓度为7.5~30 mg/mL时显示了很好的促HepG2细胞葡萄糖消耗能力(P0.001),叶子乙酸乙酯提取物、根部正丁醇与乙酸乙酯提取物的促葡萄糖消耗率达到了3.08、3.12、1.93,仅次于果实乙酸乙酯提取物(3.91)。此次研究为人面果抗糖尿病活性开发提供一定理论基础。     

昆仑雪菊提取物对α-葡萄糖苷酶的抑制作用

目的：探讨昆仑雪菊提取物对α-葡萄糖苷酶的抑制活性。方法：将昆仑雪菊干燥花序粉碎,分别用水提法和乙醇法制备5种提取物。采用α-葡萄糖苷酶体外活性抑制模型,测定昆仑雪菊的5种提取物对α-葡萄糖苷酶的抑制活性。结果：这5种提取物对α-葡萄糖苷酶活性有较强的抑制作用,抑制活性均高于阿卡波糖。其中提取物Ⅰ的抑制活性最强,IC50=28.2 mg/L。结论：昆仑雪菊提取物具有较高的α-葡萄糖苷酶抑制活性,提示昆仑雪菊在抗糖尿病产品开发方面具有很好的应用前景。     

葫芦茶提取物对α-葡萄糖苷酶活性的抑制作用研究

以阿卡波糖为阳性对照,半数抑制浓度(IC₅₀)为α-葡萄糖苷酶抑制活性评价指标,采用体外抑制模型方法评价葫芦茶醇提物不同溶剂（石油醚、乙酸乙酯、正丁醇、水）萃取物对α-葡萄糖苷酶（酵母菌来源和小鼠小肠来源）的抑制作用。经酶促动力学与Lineweaver-Burk双倒数法探讨抑制作用最强萃取物对α-葡萄糖苷酶活性的抑制机制,以期为葫芦茶有效提取物在医学、食品及化工领域的应用提供参考依据。结果表明,葫芦茶不同溶剂提取物抑制酵母、小鼠小肠来源α-葡萄糖苷酶活性强弱均为正丁醇提取物>水提取物>乙酸乙酯提取物>石油醚提取物。其中,葫芦茶正丁醇提取物对酵母菌源α-葡萄糖苷酶和小鼠小肠源α-葡萄糖苷酶的抑制作用(IC₅₀分别为13.08±1.23和221.21±3.75μg/mL)显著强于其他提取物和阳性对照阿卡波糖（P<0.05）。动力学研究表明,葫芦茶正丁醇提取物对α-葡萄糖苷酶的抑制类型为竞争性抑制。以上结果表明葫芦茶醇提物的正丁醇萃取物对α-葡萄糖苷酶活性的抑制作用较强,是挖掘抑制α-葡萄糖苷酶活性物质的主要部位。     

阿勒泰黄芪提取物对蛋白酪氨酸磷酸酯酶1B的抑制作用

本文探讨了阿勒泰黄芪不同提取物对蛋白酪氨酸磷酸酯酶1B(PTP1B)的抑制作用.采用分光光度法测定了提取物中的黄酮和皂苷含量;通过体外酶促动力学方法检测了不同提取物对PTP1B的影响,并确定了抑制类型;并采用氧化酶法检测了阿勒泰黄芪提取物对细胞利用葡萄糖能力的作用.结果表明,阿勒泰黄芪8种提取物(E1 ～8)中黄酮含量分别为5.09、10.46、3.58、3.23、53.91、21.77、5.76和7.49 mg/mL,其中E1、E2、E6、E7、E8皂苷含量分别为16.53、27.45、21.90、10.21和8.96 mg/mL;各提取物对PTP1B活性均表现出抑制作用,其中E1、E2、E7、E8的IC50分别为34.8、4.7、7.35和7.15 μg/mL,E1、E7和E8是竞争性抑制,E2是混合型竞争性抑制.E1、E2、E5、E7和E8较明显的提高了CHO-K1细胞对葡萄糖的利用.提示皂苷可能是阿勒泰黄芪抑制PTP1B活性的主要物质,通过PTP1B途径有效了提高细胞利用葡萄糖的能力.本研究为阿勒泰黄芪开发为防治糖尿病及改善胰岛素抵抗的药物或保健品提供实验依据.     

Protein Tyrosine Phosphatase 1B and α-Glucosidase Inhibitory Phlorotannins from Edible Brown Algae,Ecklonia stolonifera and Eisenia bicyclis

The present work investigates protein tyrosine phosphatase 1B (PTP1B) and the α-glucosidase inhibitory activities of two edible brown algae, Ecklonia stolonifera and Eisenia bicyclis, as well as in their isolated phlorotannins. Since the individual extracts and fractions showed significant inhibitory activities, column chromatography was performed to isolate six phlorotannins, phloroglucinol (1), dioxinodehydroeckol (2), eckol (3), phlorofurofucoeckol-A (4), dieckol (5), and 7-phloroeckol (6). Phlorotannins 3–6 were potent and noncompetitive PTP1B inhibitors with IC₅₀ values ranging from 0.56 to 2.64 μM; 4–6 exhibited the most potent α-glucosidase inhibition with IC₅₀ values ranging from 1.37 to 6.13 μM. Interestingly, 4 and 6 were noncompetitive, while 5 exhibited competitive inhibition in an α-glucosidase assay. E. stolonifera and E. bicyclis as well as their isolated phlorotannins therefore possessed marked PTP1B and α-glucosidase inhibitory activities; this could lead to opportunities in the development of therapeutic agents to control the postprandial blood glucose level and thereby prevent diabetic complications.     

A new strategy to produce active human Src from bacteria for biochemical study of its regulation

Enzymological studies of Src protein tyrosine kinase have been hindered by the lack of a suitable bacterial expression system. Poor expression of active Src appears to be due to toxicity associated with its kinase activity. To overcome this problem, we fused Src to a protein tyrosine phosphatase with an affinity tag and an appropriate thrombin cleavage site. Upon affinity purification of the fusion protein, Src was released by thrombin digestion and further purified by FPLC. This strategy has been used to produce several Src mutants that display catalytic and regulatory properties similar to those from eukaryotic expression systems. Characterization of the Src mutants confirmed that inactivation of Src by Csk through tail tyrosine phosphorylation required the Src SH3 domain.     

Inhibition of protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase by xanthones from Cratoxylum cochinchinense, and their kinetic characterization

Cratoxylum cochinchinense displayed significant inhibition against protein tyrosine phosphatase 1B (PTP1B) and α-glucosidase, both of which are key target enzymes to attenuate diabetes and obesity. The compounds responsible for both enzymes inhibition were identified as twelve xanthones (1–12) among which compounds 1 and 2 were found to be new ones. All of them simultaneously inhibited PTP1B with IC₅₀s of (2.4–52.5?µM), and α-glucosidase with IC₅₀ values of (1.7–72.7?µM), respectively. Cratoxanthone A (3) and γ-mangostin (7) were estimated to be most active inhibitors against both PTP1B (IC₅₀?=?2.4?µM for 3, 2.8?µM for 7) and α-glucosidase (IC₅₀?=?4.8?µM for 3, 1.7?µM for 7). In kinetic studies, all isolated xanthones emerged to be mixed inhibitors of α-glucosidase, whereas they behaved as competitive inhibitors of PTP1B. In time dependent experiments, compound 3 showed isomerization inhibitory behavior with following kinetic parameters: K_i^app?=?2.4?µM; k₅?=?0.05001?µM^?1?S^?1 and k₆?=?0.02076?µM^?1?S^?1.     

Synthesis, characterization, and protein tyrosine phosphatases inhibition activities of oxovanadium(IV) complexes with Schiff base and polypyridyl derivatives

Seven new mixed-ligand vanadyl complexes, [V^IVO(5-Br-SAA)(NN)] and [V^IVO(2-OH-NAA)(NN)] (1-7) (5-Br-SAA for 5-bromosalicylidene anthranilic acid, 2-OH-NAA for 2-hydroxy-1-naphthaldehyde anthranilic acid and NN for N,N′-donor heterocyclic base, namely, 2,2′-bipyridine (bpy, 1 and 5), 1,10-phenanthroline (phen, 2 and 6), dipyrido[3,2-d:2′,3′-f]quinoxaline (dpq, 3 and 7), dipyrido[3,2-a:2′,3′-c]phenazine (dppz, 4)), were synthesized and characterized. X-ray crystal structure of [V^IVO(5-Br-SAA)(phen)] revealed a distorted octahedral geometry with the Schiff base ligand coordinated in a tridentate ONO-fashion and the phenanthroline ligand in a bidentate fashion. Density-functional theory (DFT) calculations suggest a similar structure and the same coordination mode for all the other oxovanadium complexes synthesized. Biochemical assays demonstrate that the mixed-ligand oxovanadium(IV) complexes are potent inhibitors of protein tyrosine phosphatase 1B (PTP1B), with IC₅₀ values approximately 41-75 nM. Kinetics assays suggest that the complexes inhibit PTP1B in a competitive manner. Notably, they had moderate selectivity of PTP1B over T-cell protein tyrosine phosphatase (TCPTP) (about 2-fold) and good selectivity over Src homology phosphatase 1 (SHP-1) (about 4∼7-fold). Thus, these mixed-ligand complexes represent a promising class of PTP1B inhibitors for future development as anti-diabetic agents.     

Ternary oxovanadium(IV) complexes of ONO-donor Schiff base and polypyridyl derivatives as protein tyrosine phosphatase inhibitors: synthesis, characterization, and biological activities

Abstract  A series of oxovanadium complexes with mixed ligands, a tridentate ONO-donor Schiff base ligand [viz., salicylidene anthranilic acid (SAA)], and a bidentate NN ligand [viz., 2,2′-bipyridine (bpy), 1,10-phenanthroline (phen), dipyrido[3,2-d:2′,3′-f]quinoxaline (dpq), dipyrido[3,2-a:2′,3′-c]phenazine (dppz), or 7-methyldipyrido[3,2-a:2′,3′-c]phenazine (dppm)], have been synthesized and characterized by elemental analysis, electrospray ionization mass spectrometry, UV–vis spectroscopy, Fourier transform IR spectroscopy, EPR spectroscopy, and X-ray crystallography. Crystal structures of both complexes, [V^IVO(SAA)(bpy)]·0.25bpy and [V^IVO(SAA)(phen)]·0.33H₂O, reveal that oxovanadium(IV) is coordinated with one nitrogen and two oxygen atoms from the Schiff base and two nitrogen atoms from the bidentate planar ligands, in a distorted octahedral geometry (VO₃N₃). The oxidation state of V(IV) with d ¹ configuration was confirmed by EPR spectroscopy. The speciation of VO–SAA–bpy in aqueous solution was investigated by potentiomtreic pH titrations, and the results revealed that the main species are two ternary complexes at a pH range of 7.0–7.4, and one is the isolated crystalline complex. The complexes have been found to be potent inhibitors against human protein tyrosine phosphatase 1B (PTP1B) (IC₅₀ approximately 30–61 nM), T-cell protein tyrosine phosphatase (TCPTP), and Src homology phosphatase 1 (SHP-1) in vitro. Interestingly, the [V^IVO(SAA)(bpy)] complex selectively inhibits PTP1B over the other two phosphatases (approximate ninefold selectivity against SHP-1 and about twofold selectivity against TCPTP). Kinetics assays suggest that the complexes inhibit PTP1B in a competitive and reversible manner. These suggest that the complexes may be promising candidates as novel antidiabetic agents. Graphical Abstract   Electronic supplementary material  The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

Protein tyrosine phosphatase interacting protein 51 (PTPIP51) mRNA expression and localization and its in vitro interacting partner protein tyrosine phosphatase 1B (PTP1B) in human placenta of the first, second, and third trimester

The cellular localization of protein tyrosine phosphatase 51 (PTPIP51) and its in vitro interacting partner protein tyrosine phosphatase 1B (PTP1B) was studied in human placentae of different gestational stages. The expression of PTPIP51 protein and mRNA was observed in the syncytiotrophoblast and cytotrophoblast layer of placentae from the first, second, and third trimesters. In contrast, PTP1B expression was restricted to the syncytiotrophoblast during all gestational stages. Cells of the cytotrophoblasts and parts of the syncytiotrophoblasts expressing high amounts of PTPIP51 were found to execute apoptosis as shown by TdT-mediated dUTP-biotin nick end labeling assay, cytokeratin 18f, and caspase 3 expression. PTPIP51 could also be traced in the endothelium and smooth muscle cells of placental arterial and venous vessels, identified by double immunostainings with antibodies directed against van Willebrand factor and alpha-smooth muscle actin. Some of these cells showing a high PTPIP51 reactivity were Ki67 positive, indicating proliferation. Additionally, a small population of placental CD14-positive macrophages and mesenchymal cells within the villous stroma were detected as PTPIP51 positive. Our data suggest that both proteins, PTPIP51 and PTP1B, play a role in differentiation and apoptosis of the cytotrophoblast and syncytiotrophoblast, respectively. Moreover, PTPIP51 may also serve as a cellular signaling partner in angiogenesis and vascular remodeling.     

Anthocyanins from flowers of Cichorium intybus

From the blue perianth segments of Cichorium intybus we isolated four anthocyanins. The pigments were identified as delphinidin 3,5-di-O-(6-O-malonyl-beta-D-glucoside) and delphinidin 3-O-(6-O-malonyl-beta-D-glucoside)-5-O-beta-D-glucoside and the known compounds were delphinidin 3-O-beta-D-glucoside-5-O-(6-O-malonyl-beta-D-glucoside) and delphinidin 3,5-di-O-beta-D-glucoside. In addition 3-O-p-coumaroyl quinic acid has been identified.     

Evaluation of licorice flavonoids as protein tyrosine phosphatase 1B inhibitors

Protein tyrosine phosphatase 1B (PTP1B) is a major negative regulator in insulin- and leptin-signaling cascades as well as a positive regulator in tumorigenesis, and much attention has been paid to PTP1B inhibitors as potential therapies for diabetes, obesity, and cancer. In the present study, the screening of a compound library of licorice flavonoids allowed for the discovery of several compounds, including licoagrone (3), licoagrodin (4), licoagroaurone (5), and isobavachalcone (6), as new PTP1B inhibitors. It was revealed that these compounds inhibit the activity of PTP1B in different modes and with different selectivities and that they exhibit different cellular activity in the insulin-signaling pathway. Glycybenzofuran (1), a competitive PTP1B inhibitor, showed both excellent inhibitory selectivity against PTP1B and cellular activity on the insulin-stimulated Akt phosphorylation level. The similarity of its action profiling in the insulin-signaling pathway suggested its potential as a new anti-insulin-resistant drug candidate.